Information on EC 1.7.2.3 - trimethylamine-N-oxide reductase (cytochrome c)

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
1.7.2.3
-
RECOMMENDED NAME
GeneOntology No.
trimethylamine-N-oxide reductase (cytochrome c)
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
NADH + H+ + trimethylamine N-oxide = NAD+ + trimethylamine + H2O
show the reaction diagram
trimethylamine + 2 (ferricytochrome c)-subunit + H2O = trimethylamine N-oxide + 2 (ferrocytochrome c)-subunit + 2 H+
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
formate to trimethylamine N-oxide electron transfer
-
-
hydrogen to trimethylamine N-oxide electron transfer
-
-
NADH to trimethylamine N-oxide electron transfer
-
-
SYSTEMATIC NAME
IUBMB Comments
trimethylamine:cytochrome c oxidoreductase
The cytochrome c involved in photosynthetic bacteria is a pentaheme protein. Contains bis(molybdopterin guanine dinucleotide)molybdenum cofactor. The reductant is a membrane-bound multiheme cytochrome c. Also reduces dimethyl sulfoxide to dimethyl sulfide.
CAS REGISTRY NUMBER
COMMENTARY hide
37256-34-1
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
wild-type strain ES114, and mutant strains strains JB1, AMJ2, and KV1585
-
-
Manually annotated by BRENDA team
inducible
-
-
Manually annotated by BRENDA team
strain Och 114
-
-
Manually annotated by BRENDA team
Erythrobacter sp. Och 114
strain Och 114
-
-
Manually annotated by BRENDA team
Hawaiian bobtail squid
-
-
Manually annotated by BRENDA team
a single enzyme responsible for both trimethylamine-N-oxide and dimethylsulfoxide reductase
-
-
Manually annotated by BRENDA team
strain MR1
SwissProt
Manually annotated by BRENDA team
marine bacterium, 2 enzyme forms
-
-
Manually annotated by BRENDA team
symbiotic bacterium associated with the light organ of the adult Hawaiian bobtail squid Euprymna scolopes, construction of different mutant strains lacking torECA, torYZ, or dmsABC gene activity, the strain lacking all three enzymes is designated as AKD806
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-chloropyridine N-oxide + electron donor
2-chloropyridine + oxidized electron donor + H2O
show the reaction diagram
-
-
-
?
3-hydroxypyridine N-oxide + electron donor
3-hydroxypyridine + oxidized electron donor + H2O
show the reaction diagram
-
-
-
?
3-picoline N-oxide + electron donor
3-picoline + oxidized electron donor + H2O
show the reaction diagram
-
-
-
?
4-chloropyridine N-oxide + electron donor
4-chloropyridine + oxidized electron donor + H2O
show the reaction diagram
-
-
-
?
4-methylmorpholine N-oxide + electron donor
4-methylmorpholine + oxidized electron donor + H2O
show the reaction diagram
4-methylmorpholine-N-oxide + (ferrocytochrome c)-subunit + H+
4-methylmorpholine + (ferricytochrome c)-subunit + H2O
show the reaction diagram
-
-
-
-
?
adenosine N-oxide + electron donor
adenosine + H2O + oxidized electron donor
show the reaction diagram
alpha-picoline N-oxide + electron donor
alpha-picoline + H2O + oxidized electron donor
show the reaction diagram
biotin sulfoxide + (ferrocytochrome c)-subunit
? + (ferrocytochrome c)-subunit
show the reaction diagram
-
-
-
-
?
bromate + (ferrocytochrome c)-subunit
? + (ferricytochrome c)-subunit
show the reaction diagram
-
-
-
-
?
chlorate + electron donor
?
show the reaction diagram
dimethylsulfoxide + (ferrocytochrome c)-subunit + 2 H+
dimethylsulfide + (ferricytochrome c)-subunit + H2O
show the reaction diagram
dimethylsulfoxide + electron donor
? + oxidized electron donor + H2O
show the reaction diagram
diphenylsulfoxide + electron donor
diphenylsulfide + oxidized electron donor + H2O
show the reaction diagram
gamma-picoline N-oxide + electron donor
gamma-picoline + H2O + oxidized electron donor
show the reaction diagram
hydroxylamine + (ferrocytochrome c)-subunit
? + (ferricytochrome c)-subunit
show the reaction diagram
-
-
-
-
?
hydroxylamine N-oxide + electron donor
hydroxylamine + H2O + oxidized electron donor
show the reaction diagram
L-methionine sulfoxide + electron donor
L-methionine + oxidized electron donor + H2O
show the reaction diagram
N,N-dimethyldodecylamine N-oxide + electron donor
N,N-dimethyldodecylamine + H2O + oxidized electron donor
show the reaction diagram
N,N-dimethylhexylamine N-oxide + electron donor
N,N-dimethylhexylamine + oxidized electron donor + H2O
show the reaction diagram
-
-
-
?
N-cyclohexyldimethylamine N-oxide + electron donor
N-cyclohexyldimethylamine + oxidized electron donor + H2O
show the reaction diagram
-
-
-
?
nicotinic acid N-oxide + (ferrocytochrome c)-subunit + H+
nicotinic acid + (ferricytochrome c)-subunit + H2O
show the reaction diagram
-
-
-
-
?
picoline N-oxide + (ferrocytochrome c)-subunit + H+
picoline + (ferricytochrome c)-subunit + H2O
show the reaction diagram
-
-
-
-
?
pyridine N-oxide + electron donor
pyridine + oxidized electron donor + H2O
show the reaction diagram
tetramethylene sulfoxide + (ferrocytochrome c)-subunit + H+
? + (ferricytochrome c)-subunit
show the reaction diagram
-
-
-
-
?
tetramethylene sulfoxide + electron donor
tetrahydrothiophene + oxidized electron donor + H2O
show the reaction diagram
-
tungsten-substituted enzyme
-
?
trimethylamine N-oxide + (ferrocytochrome c)-subunit + H+
trimethylamine + (ferricytochrome c)-subunit + H2O
show the reaction diagram
trimethylamine N-oxide + electron donor
trimethylamine + oxidized electron donor + H2O
show the reaction diagram
trimethylamine N-oxide + NADH
NAD+ + trimethylamine + H2O
show the reaction diagram
trimethylamine-N-oxide + electron donor
trimethylamine + oxidized electron donor + H2O
show the reaction diagram
trimethylamine-N-oxide + enzyme-MoIV
trimethylamine + enzyme-MoVI + H2O
show the reaction diagram
-
anaerobic respiration
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
trimethylamine N-oxide + (ferrocytochrome c)-subunit + H+
trimethylamine + (ferricytochrome c)-subunit + H2O
show the reaction diagram
trimethylamine N-oxide + NADH
NAD+ + trimethylamine + H2O
show the reaction diagram
-
enzyme is highly specific for trimethylamine oxide as alternative terminal electron acceptor
-
-
?
trimethylamine-N-oxide + electron donor
trimethylamine + oxidized electron donor + H2O
show the reaction diagram
trimethylamine-N-oxide + enzyme-MoIV
trimethylamine + enzyme-MoVI + H2O
show the reaction diagram
-
anaerobic respiration
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cytochrome c
FAD
-
stimulation
FMN
-
stimulation
molybdenum cofactor
-
-
molybdopterin
-
-
molybdopterin guanine dinucleotide
-
-
additional information
-
the enzyme contains more than 0.4 atoms of acid-labile sulfur per molecular weight of 200000
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe-S cluster
-
-
Molybdenum
molybdopterin
-
in the molybdopterin molybdenum cofactor, Mo-S and Mo-O interactions, molecular structure modelling, overview
Zinc
-
enzyme contains 1.52 atoms of zinc
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
2,2-dipyridyl
-
slight
5,5'-dithiobis(2-nitrobenzoate)
-
-
DTT
-
inhibits cytochrome c formation
EGTA
-
38% inhibition at 10 mM
FAD
-
inhibition, when added to the standard assay mixture containing benzyl viologen as electron acceptor
FMN
-
inhibition, when added to the standard assay mixture containing benzyl viologen as electron acceptor
iodoacetate
-
partial
N-ethylmaleimide
-
both inducible and constitutive enzyme are affected equally at 5 mM
Na2MoO4
-
-
Na2WO4
-
-
p-chloromercuribenzoate
Sodium chlorate
-
partial
Urea
-
50% inhibition at 6 mM
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
TorD
-
at 42C and in the absence of TorD TorA is poorly matured and almost completely degraded
-
additional information
-
the enzyme is induced in the presence of trimethylamine oxide mainly during exponential phase
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.01
2-chloropyridine N-oxide
-
-
0.75
3-hydroxypyridine N-oxide
-
-
5.43
3-picoline N-oxide
-
-
2.15
4-chloropyridine N-oxide
-
-
0.00754 - 1.4
4-methylmorpholine N-oxide
0.00991 - 0.653
alpha-picoline N-oxide
0.33
benzyl viologen
-
with trimethylamine N-oxide
0.36
biotin sulfoxide
-
-
0.67 - 6
Dimethylsulfoxide
0.0278
diphenylsulfoxide
-
tungsten-restored enzyme
0.00838 - 6.95
gamma-picoline N-oxide
7.39 - 11.8
hydroxylamine N-oxide
0.15
methyl viologen
-
with trimethylamine N-oxide, pH 6.9
1 - 2.41
N,N-dimethyldodecylamine N-oxide
1.14
N,N-dimethylhexylamine N-oxide
-
-
4.74
N-cyclohexyldimethylamine N-oxide
-
-
0.0108 - 2.25
Pyridine N-oxide
0.0252 - 3.37
tetramethylene sulfoxide
0.006 - 1.44
Trimethylamine N-oxide
0.3 - 24
Trimethylamine-N-oxide
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
101
2-chloropyridine N-oxide
Escherichia coli
-
-
49.2
3-hydroxypyridine N-oxide
Escherichia coli
-
-
137
3-picoline N-oxide
Escherichia coli
-
-
66.7
4-chloropyridine N-oxide
Escherichia coli
-
-
52.2 - 109
4-methylmorpholine N-oxide
54.7 - 102
alpha-picoline N-oxide
4
dibutylsulfoxide
40.2
Dimethylsulfoxide
Escherichia coli
-
tungsten-restored enzyme
4 - 26.8
diphenylsulfoxide
49.6 - 57.2
gamma-picoline N-oxide
43.6 - 70.6
hydroxylamine N-oxide
151 - 155
N,N-dimethyldodecylamine N-oxide
13.8
N,N-dimethylhexylamine N-oxide
Escherichia coli
-
-
45.6
N-cyclohexyldimethylamine N-oxide
Escherichia coli
-
-
42.2 - 53.5
Pyridine N-oxide
56
tetramethylene sulfoxide
Escherichia coli
-
tungsten-restored enzyme
58 - 258
Trimethylamine N-oxide
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.096
-
anaerobic growth conditions, grown without trimethylamine N-oxide
0.13
-
periplasmic fraction
0.163
-
microaerobic growth conditions, grown without trimethylamine N-oxide
0.25
-
aerobic growth conditions, grown with trimethylamine N-oxide
0.374
-
anaerobic growth conditions, grown with trimethylamine N-oxide
0.41
-
mutants, which reduce little or no trimethylamine N-oxide in vivo, but their extracts retain full capacity to reduce it with methyl viologen, formate as electron donor
0.56
-
microaerobic growth conditions, grown with trimethylamine N-oxide
0.66
-
mutants partially defective in trimethylamine N-oxide reductase activity, which lack the inducible enzyme but retain the constitutive activity, FMN or vitamin K5 as electron donor
1.29
-
mutants partially defective in trimethylamine N-oxide reductase activity, which lack the inducible enzyme but retain the constitutive activity, formate as electron donor
1.56
-
wild-type strain, formate as electron donor
2.63
-
mutants, which reduce little or no trimethylamine N-oxide in vivo, but their extracts retain full capacity to reduce it with methyl viologen, vitamin K5 as electron donor
3.73
-
wild-type strain, vitamin K5 as electron donor
3.77
-
mutants, which reduce little or no trimethylamine N-oxide in vivo, but their extracts retain full capacity to reduce it with methyl viologen, FMN as electron donor
4.31
-
mutants partially defective in trimethylamine N-oxide reductase activity, which lack the inducible enzyme but retain the constitutive activity, methyl viologen as electron donor
4.7
-
wild-type strain, FMN as electron donor
9.92
-
wild-type strain, methyl viologen as electron donor
10.2
-
purified enzyme
11.2
-
mutants, which reduce little or no trimethylamine N-oxide in vivo, but their extracts retain full capacity to reduce it with methyl viologen, methyl viologen as electron donor
33
-
purified enzyme, assay performed in 100 mM phosphate buffer, pH 6.8 with a trimethylamine N-oxide concentration 0.5 mM and a concentration 20 mM of 2-hydroxypyridine N-oxide
34
-
purified enzyme, assay performed in 100 mM phosphate buffer, pH 6.8 with a trimethylamine N-oxide concentration 0.5 mM
35
-
purified enzyme, assay performed in 100 mM phosphate buffer, pH 6.8 with a trimethylamine N-oxide concentration 0.5 mM and a concentration 20 mM of tetramethylenesulfoxide
36
-
purified enzyme, assay performed in 100 mM phosphate buffer, pH 6.8 with a trimethylamine N-oxide concentration 0.5 mM and a concentration 20 mM of picolinic acid N-oxide or a concentration 20 mM of dimethylsulfoxide
41
-
purified tungsten-substituted enzyme
70
-
30 mM trimethylamine N-oxide, cell free extract, aerobic conditions
105
-
purified enzyme, with trimethylamine N-oxide as substrate
250
-
purified enzyme
320
-
30 mM trimethylamine N-oxide, cell free extract, anaerobic conditions
1350
-
crude extract of mutant strain lacking the TorD protein
1720
-
crude extract of wild-type strain
1810
-
crude extract of mutant strain lacking the TorD protein but complemented by pTorD
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 5.5
-
for molybdoenzyme
5
-
for tungsten-substituted enzyme, a significant decrease in activity is found at pH 5.5
6.9
-
with methyl viologen
7
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
assay at
37
-
assay at
60
-
for molybdoenzyme, maximal activity remains the same at 80C
80
-
for tungsten-substituted enzyme, maximal level above
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
24100
-
monomeric form, small-angle X-ray scattering
24350 - 24360
-
monomeric form, mass spectrometry and sedimentation equilibrium analysis
47000
-
2 MW forms, MW: 47000, SDS-PAGE in absence of reducing agents and MW: 84000, gel filtration, SDS-PAGE under reducing conditions
47800
-
dimeric form, small-angle X-ray scattering
48710
-
dimeric form, mass spectrometry and sedimentation equilibrium analysis
80000
-
SDS-PAGE
83000
-
gel electrophoresis
84000
-
2 MW forms, MW: 47000, SDS-PAGE in absence of reducing conditions and MW: 84000, gel filtration, SDS-PAGE under reducing conditions
85030
-
calculated from amino acid sequence; electrospray mass spectroscopy
87000
-
gel filtration
95000
-
gradient gel electrophoresis, gel isoelectric focusing
110000
-
a single inducible trimethylamine-N-oxide reductase which can exist as a dimer, MW: 230000, or a monomer, MW: 110000, gel filtration
172000
-
gel filtration
200000
-
gel filtration
230000
-
a single inducible trimethylamine-N-oxide reductase which can exist as a dimer, MW: 230000 or a monomer, MW: 110000, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 22500, recombinant enzyme, SDS-PAGE
monomer
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method
recombinant monomeric, dimeric, and trimeric forms, hanging drop vapour diffusion method, 4C, 0.001 ml of 1.2 mg/ml protein in 20 mM Tris-HCl, pH 8.0, 220 mM NaCl, 10 mM DTT, mixed with equal volume of reservoir solution containing 1.6 M ammonium sulfate, 100 mM MES, pH 6.4, 4-6 days, cryoprotection by addition of 15% w/v ethylene glycerol to the reservoir solution, X-ray diffraction structure determination and analysis at 2.42 A resolution
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 8.5
-
stability peak at pH 7.3
392755
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
-
20 min, 10% loss of activity
65
-
5 min, 90% loss of constitutive activity, 10% loss of inducible activity
70
-
30 min, enzyme activity does not change
90
-
10 min, pH 7.3, complete loss of activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
about 50% of the activity of the molybdoenzyme is lost in the presence of 0.1 M NaCl, only about 4% of its initial activity is left in the presence of 2 M NaCl, 15% of the initial activity of the tungsten-substituted enzyme is left at 2 M NaCl
-
activity is easily lost on dialysis
-
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
aeration for 10 min causes 10% inactivation
-
392756
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80C stable for several months
-
-80C, 10% loss of activity after 15 days
-
-80C, 45% loss of activity after 30 days
-
-80C, inducible and constitutive enzyme, 10% loss of activity after 15 days
-
0C, 50 mM sodium phosphate buffer, pH 7.3, 30% loss of activity after 17 days
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
HiTrap Chelating HP column chromatography
-
HiTrap Q FF column chromatography; recombinant His-tagged enzyme by nickel affinity and anion exchange chromatography
-
of 2 enzyme forms, using ammonium sulfate treatment, ion exchange buffer treatment, column chromatography on DEAE-Sepharose CL6B and hydroxyapatite and gel filtration on Sephacryl S-300
-
recombinant His-tagged enzyme from strain BL21(DE3) to near homogeneity
-
recombinant His-tagged monomeric, dimeric, and trimeric forms from Escherichia coli strain BL21(DE3) to homogeneity by nickel affinity chromatography, and gel filtration for the the monomeric form
-
using ammonium sulfate treatment and chromatography on Sephacryl S-200 column and Mono-Q column
-
using heat treatment, ammonium sulfate precipitation and chromatography on Bio-Gel A-1.5m, DEAE-cellulose and reactive blue-agarose
-
using heat treatment, column chromatography on DEAE-cellulose, Sephadex G-200, DEAE-Sepharose CL-6B and hydroxyapatite
-
using ion exchange chromatography on DE52 column, chromatography on a Mono Q HR 16/10 column and preparative electrophoresis
using ion exchange chromatography on DE52, chromatography on a Mono Q HR 16/10 column and preparative electrophoresis
-
using polyethyleneimine to remove nucleic acids, ammonium sulfate treatment, column chromatography on DEAE-Sephacel and Bio-Gel A-5m, chromatofocusing and chromatography on Sephacryl-S-300 column
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
amplification of the structural torA gene encoding the enzyme and iits flanking regions using PCR techniques, the torA gene is the third gene of a TMAO-inducible operon, torECAD, encoding the TMAO respiratory components, the torC gene encodes a pentahemic c-type cytochrome, likely to be involved in electron transfer to the TorA terminal reductase, the role of the torE gene is unknown, torD gene encodes the TorD protein, a cytoplasmic protein involved in the folding process of the TorA precursor protein
expressed in Escherichia coli
-
expressed in Escherichia coli; overexpression as His-tagged protein
-
expression in strain BL21(DE3) as His-tagged protein
-
fusion protein with beta-galactosidase
-
gene torA, the torCAD operon encodes the Tor system induced in the presence of trimethylamine oxide mainly during exponential phase
-
gene torD, DNA sequence determination and analysis, overexpression in Escherichia coli strain BL21(DE3) as His-tagged protein
-
GFP-tagged enzyme expression, the genome sequence of Vibrio fischeri reveals three putative TMAO reductase operons, transcriptional regulation, overview
-
overexpression
-
the torECA promoter, and to a lesser extent the torYZ and dmsABC promoters, are active during symbiotic colonization of juvenile Euprymna scolopes, transcriptional regulation, overview
-
the trimethylamine N-oxide reductase respiratory system is encoded by the torECAD operon, a three-gene cluster, torSTR, encoding a complex two-component regulatory system is present downstream of the torECAD operon, introduction of the torSTR gene cluster into Escherichia coli shows that this regulatory gene cluster is involved in trimethylamine N-oxide induction of the torE promoter, the torR operator site is required for induction of the tor structural promoter, TorS of Escherichia coli , the trimethylamine N-oxide sensor of Escherichia coli is able to transphosphorylate TorR of Shewanella oneidensis, the trimethylamine N-oxide response regulator of Shewanella oneidensis
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
Show AA Sequence (977 entries)
Please use the Sequence Search for a certain query.